{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T23:14:48Z","timestamp":1791328488926,"version":"4.3.1"},"reference-count":70,"publisher":"Public Library of Science (PLoS)","issue":"6","license":[{"start":{"date-parts":[[2016,6,6]],"date-time":"2016-06-06T00:00:00Z","timestamp":1465171200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"publisher","award":["R01 AG019322"],"award-info":[{"award-number":["R01 AG019322"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000066","name":"National Institute of Environmental Health Sciences","doi-asserted-by":"publisher","award":["R01 ES020718"],"award-info":[{"award-number":["R01 ES020718"]}],"id":[{"id":"10.13039\/100000066","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100001671","name":"Hereditary Disease Foundation","doi-asserted-by":"publisher","award":["Research Contract"],"award-info":[{"award-number":["Research Contract"]}],"id":[{"id":"10.13039\/100001671","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0155747","type":"journal-article","created":{"date-parts":[[2016,6,6]],"date-time":"2016-06-06T17:31:53Z","timestamp":1465234313000},"page":"e0155747","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":58,"title":["Folding Landscape of Mutant Huntingtin Exon1: Diffusible Multimers, Oligomers and Fibrils, and No Detectable Monomer"],"prefix":"10.1371","volume":"11","author":[{"given":"Bankanidhi","family":"Sahoo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Irene","family":"Arduini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kenneth W.","family":"Drombosky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ravindra","family":"Kodali","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laurie H.","family":"Sanders","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J. Timothy","family":"Greenamyre","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ronald","family":"Wetzel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2016,6,6]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/j.tibs.2013.05.003","article-title":"Huntington's disease: underlying molecular mechanisms and emerging concepts","volume":"38","author":"J Labbadia","year":"2013","journal-title":"Trends Biochem Sci"},{"key":"ref2","article-title":"Huntington's Disease","author":"G Bates","year":"2014"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"15005","DOI":"10.1038\/nrdp.2015.5","article-title":"Huntington disease","author":"GP Bates","year":"2015","journal-title":"Nature Reviews Disease Primers"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1093\/hmg\/ddu504","article-title":"Comparative study of naturally occurring huntingtin fragments in Drosophila points to exon 1 as the most pathogenic species in Huntington's disease","volume":"24","author":"BA Barbaro","year":"2015","journal-title":"Hum Mol Genet"},{"key":"ref5","first-page":"274","article-title":"Huntington's Disease","author":"R Wetzel","year":"2014"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1038\/378403a0","article-title":"Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias","volume":"378","author":"Y Trottier","year":"1995","journal-title":"Nature"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"16764","DOI":"10.1073\/pnas.0608175103","article-title":"Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions","volume":"103","author":"SL Crick","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"4215","DOI":"10.1093\/hmg\/ddt273","article-title":"Linear and extended: a common polyglutamine conformation recognized by the three antibodies MW1, 1C2 and 3B5H10","volume":"22","author":"FA Klein","year":"2013","journal-title":"Hum Mol Genet"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"11634","DOI":"10.1073\/pnas.182393899","article-title":"A linear lattice model for poly-glutamine in CAG expansion diseases","volume":"99","author":"MJ Bennett","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"2507","DOI":"10.1016\/j.jmb.2015.05.023","article-title":"Anti-PolyQ Antibodies Recognize a Short PolyQ Stretch in Both Normal and Mutant Huntingtin Exon 1","volume":"427","author":"GE Owens","year":"2015","journal-title":"J Mol Biol"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"15916","DOI":"10.1074\/jbc.M511007200","article-title":"Expression and characterization of full-length human huntingtin, an elongated HEAT repeat protein","volume":"281","author":"W Li","year":"2006","journal-title":"J Biol Chem"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"e0121055","DOI":"10.1371\/journal.pone.0121055","article-title":"Scalable production in human cells and biochemical characterization of full-length normal and mutant huntingtin","volume":"10","author":"B Huang","year":"2015","journal-title":"PLoS ONE"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"13487","DOI":"10.1074\/jbc.M111.286609","article-title":"Native mutant huntingtin in human brain: evidence for prevalence of full-length monomer","volume":"287","author":"E Sapp","year":"2012","journal-title":"J Biol Chem"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"21807","DOI":"10.1074\/jbc.M109.084434","article-title":"Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool","volume":"285","author":"MA Olshina","year":"2010","journal-title":"J Biol Chem"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1016\/j.jmb.2011.12.010","article-title":"Slow amyloid nucleation via alpha-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments","volume":"415","author":"M Jayaraman","year":"2012","journal-title":"J Mol Biol"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"4285","DOI":"10.1021\/acs.biochem.5b00478","article-title":"Huntingtin N-Terminal Monomeric and Multimeric Structures Destabilized by Covalent Modification of Heteroatomic Residues","volume":"54","author":"JR Arndt","year":"2015","journal-title":"Biochem"},{"key":"ref17","first-page":"323","article-title":"Huntington's Disease","author":"A Hughes","year":"2014"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1038\/nsmb.1570","article-title":"Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism","volume":"16","author":"AK Thakur","year":"2009","journal-title":"Nat Struct Mol Biol"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1016\/j.jmb.2012.01.030","article-title":"Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence","volume":"421","author":"R Wetzel","year":"2012","journal-title":"J Mol Biol"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/S0092-8674(00)80514-0","article-title":"Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo","volume":"90","author":"E Scherzinger","year":"1997","journal-title":"Cell"},{"key":"ref21","first-page":"429","article-title":"Huntington's Disease","author":"GP Bates","year":"2002"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1016\/S0092-8674(00)81467-1","article-title":"A critical role for amino-terminal glutamine\/asparagine repeats in the formation and propagation of a yeast prion","volume":"93","author":"AH DePace","year":"1998","journal-title":"Cell"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"1990","DOI":"10.1126\/science.277.5334.1990","article-title":"Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain","volume":"277","author":"M DiFiglia","year":"1997","journal-title":"Science"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1016\/S0092-8674(00)80513-9","article-title":"Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation","volume":"90","author":"SW Davies","year":"1997","journal-title":"Cell"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"10417","DOI":"10.1073\/pnas.152161099","article-title":"The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans","volume":"99","author":"JF Morley","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"4604","DOI":"10.1073\/pnas.96.8.4604","article-title":"Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology","volume":"96","author":"E Scherzinger","year":"1999","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1006\/jmbi.2001.4850","article-title":"Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity","volume":"311","author":"S Chen","year":"2001","journal-title":"J Mol Biol"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1038\/nature02998","article-title":"Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death","volume":"431","author":"M Arrasate","year":"2004","journal-title":"Nature"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"1602","DOI":"10.1093\/hmg\/ddu574","article-title":"Disruption of the nuclear membrane by perinuclear inclusions of mutant huntingtin causes cell-cycle re-entry and striatal cell death in mouse and cell models of Huntington's disease","volume":"24","author":"KY Liu","year":"2015","journal-title":"Hum Mol Genet"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"41032","DOI":"10.1074\/jbc.M205809200","article-title":"Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization","volume":"277","author":"MA Poirier","year":"2002","journal-title":"J Biol Chem"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"846","DOI":"10.1111\/j.1471-4159.2007.05032.x","article-title":"Sensitive biochemical aggregate detection reveals aggregation onset before symptom development in cellular and murine models of Huntington's disease","volume":"104","author":"A Weiss","year":"2008","journal-title":"J Neurochem"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"e44457","DOI":"10.1371\/journal.pone.0044457","article-title":"Fragments of HdhQ150 mutant huntingtin form a soluble oligomer pool that declines with aggregate deposition upon aging","volume":"7","author":"D Marcellin","year":"2012","journal-title":"PLoS ONE"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"2753","DOI":"10.1038\/ncomms3753","article-title":"Soluble forms of polyQ-expanded huntingtin rather than large aggregates cause endoplasmic reticulum stress","volume":"4","author":"J Leitman","year":"2013","journal-title":"Nat Commun"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1093\/hmg\/ddp467","article-title":"Identical oligomeric and fibrillar structures captured from the brains of R6\/2 and knock-in mouse models of Huntington's disease","volume":"19","author":"K Sathasivam","year":"2010","journal-title":"Hum Mol Genet"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1017\/S0033583515000219","article-title":"Delayed emergence of subdiffraction-sized mutant huntingtin fibrils following inclusion body formation","author":"SJ Sahl","year":"2015","journal-title":"Q Rev Biophys"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"3308","DOI":"10.1101\/gad.1673408","article-title":"Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity","volume":"22","author":"ML Duennwald","year":"2008","journal-title":"Genes Dev"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"3897","DOI":"10.1021\/bi500300c","article-title":"Aggregation behavior of chemically synthesized, full-length huntingtin exon1","volume":"53","author":"B Sahoo","year":"2014","journal-title":"Biochem"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"2767","DOI":"10.1021\/cb500335w","article-title":"Super-resolution fluorescence of Huntingtin reveals growth of globular species into short fibers and coexistence of distinct aggregates","volume":"9","author":"WC Duim","year":"2014","journal-title":"ACS chemical biology"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"3078","DOI":"10.1016\/j.bpj.2010.02.058","article-title":"A two-step path to inclusion formation of huntingtin peptides revealed by number and brightness analysis","volume":"98","author":"G Ossato","year":"2010","journal-title":"Biophys J"},{"key":"ref40","first-page":"67","article-title":"Protein amyloid aggregation: Methods and protocols. Methods in Molecular Biology","volume":"1345","author":"B Sahoo","year":"2015"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"2855","DOI":"10.1016\/j.bpj.2011.11.012","article-title":"Fluorescence correlation spectroscopy: past, present, future","volume":"101","author":"EL Elson","year":"2011","journal-title":"Biophys J"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"10123","DOI":"10.1073\/pnas.96.18.10123","article-title":"Rapid characterization of green fluorescent protein fusion proteins on the molecular and cellular level by fluorescence correlation microscopy","volume":"96","author":"R Brock","year":"1999","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"L55","DOI":"10.1529\/biophysj.106.101485","article-title":"Detecting amyloid-beta aggregation with fiber-based fluorescence correlation spectroscopy","volume":"92","author":"K Garai","year":"2007","journal-title":"Biophys J"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"6043","DOI":"10.1073\/pnas.95.11.6043","article-title":"Intranuclear diffusion and hybridization state of oligonucleotides measured by fluorescence correlation spectroscopy in living cells","volume":"95","author":"JC Politz","year":"1998","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"90801","DOI":"10.1117\/1.JBO.19.9.090801","article-title":"Measuring protein dynamics in live cells: protocols and practical considerations for fluorescence fluctuation microscopy","volume":"19","author":"RT Youker","year":"2014","journal-title":"Journal of biomedical optics"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/S1074-5521(97)90255-6","article-title":"Observation of metastable Abeta amyloid protofibrils by atomic force microscopy","volume":"4","author":"JD Harper","year":"1997","journal-title":"Chem Biol"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1016\/j.nbd.2004.04.001","article-title":"A cell-based screen for drugs to treat Huntington's disease","volume":"16","author":"CT Aiken","year":"2004","journal-title":"Neurobiol Dis"},{"key":"ref48","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms6659","article-title":"The role of protein clearance mechanisms in organismal ageing and age-related diseases","volume":"5","author":"D Vilchez","year":"2014","journal-title":"Nature Commun"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1006\/meth.2000.1054","article-title":"Analysis of gene-specific DNA damage and repair using quantitative polymerase chain reaction","volume":"22","author":"S Ayala-Torres","year":"2000","journal-title":"Methods"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/j.nbd.2013.10.013","article-title":"LRRK2 mutations cause mitochondrial DNA damage in iPSC-derived neural cells from Parkinson's disease patients: reversal by gene correction","volume":"62","author":"LH Sanders","year":"2014","journal-title":"Neurobiol Dis"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"2859","DOI":"10.1093\/hmg\/9.19.2859","article-title":"Intranuclear huntingtin increases the expression of caspase-1 and induces apoptosis","volume":"9","author":"SH Li","year":"2000","journal-title":"Hum Mol Genet"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1002\/ana.410410514","article-title":"Oxidative damage and metabolic dysfunction in Huntington's disease: selective vulnerability of the basal ganglia","volume":"41","author":"SE Browne","year":"1997","journal-title":"Ann Neurol"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"2560","DOI":"10.1074\/jbc.M114.603332","article-title":"Molecular interaction between the chaperone Hsc70 and the N-terminal flank of Huntingtin exon 1 modulates aggregation","volume":"290","author":"E Monsellier","year":"2015","journal-title":"J Biol Chem"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/j.jmb.2008.09.026","article-title":"Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization","volume":"384","author":"A Vitalis","year":"2008","journal-title":"J Mol Biol"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"6739","DOI":"10.1073\/pnas.110138997","article-title":"Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: implications for Huntington's disease therapy","volume":"97","author":"V Heiser","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.1073\/pnas.1521933113","article-title":"Huntingtin exon 1 fibrils feature an interdigitated beta-hairpin-based polyglutamine core","volume":"113","author":"CL Hoop","year":"2016","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"17797","DOI":"10.1073\/pnas.1113260108","article-title":"A soluble alpha-synuclein construct forms a dynamic tetramer","volume":"108","author":"W Wang","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1002\/pro.2056","article-title":"N-Terminal acetylation is critical for forming alpha-helical oligomer of alpha-synuclein","volume":"21","author":"AJ Trexler","year":"2012","journal-title":"Protein Sci"},{"key":"ref59","doi-asserted-by":"crossref","first-page":"14092","DOI":"10.1021\/bi0357816","article-title":"Abeta protofibrils possess a stable core structure resistant to hydrogen exchange","volume":"42","author":"I Kheterpal","year":"2003","journal-title":"Biochem"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1126\/science.1092194","article-title":"SUMO modification of Huntingtin and Huntington's disease pathology","volume":"304","author":"JS Steffan","year":"2004","journal-title":"Science"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"828","DOI":"10.1016\/j.neuron.2009.11.020","article-title":"Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice","volume":"64","author":"X Gu","year":"2009","journal-title":"Neuron"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1016\/j.jmb.2006.07.087","article-title":"Analysis of molecular recognition features (MoRFs)","volume":"362","author":"A Mohan","year":"2006","journal-title":"J Mol Biol"},{"key":"ref63","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1038\/nsmb.1700","article-title":"The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation","volume":"16","author":"S Tam","year":"2009","journal-title":"Nat Struct Mol Biol"},{"key":"ref64","doi-asserted-by":"crossref","first-page":"3498","DOI":"10.1073\/pnas.0308679101","article-title":"Venezuelan kindreds reveal that genetic and environmental factors modulate Huntington's disease age of onset","volume":"101","author":"NS Wexler","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref65","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1038\/ncb1830","article-title":"Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates","volume":"11","author":"PH Ren","year":"2009","journal-title":"Nat Cell Biol"},{"key":"ref66","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1038\/87842","article-title":"Polyglutamine and CBP: fatal attraction?","volume":"7","author":"A McCampbell","year":"2001","journal-title":"Nat Med"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"822","DOI":"10.1038\/nn.3721","article-title":"Inhibition of mitochondrial protein import by mutant huntingtin","volume":"17","author":"H Yano","year":"2014","journal-title":"Nat Neurosci"},{"key":"ref68","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/S0076-6879(06)13003-7","article-title":"Kinetics and thermodynamics of amyloid assembly using a high-performance liquid chromatography-based sedimentation assay","volume":"413","author":"B O'Nuallain","year":"2006","journal-title":"Methods Enzymol"},{"key":"ref69","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.jmb.2015.06.008","article-title":"C-Terminal threonine reduces A\u03b243 amyloidogenicity compared with A\u03b242","volume":"428","author":"S Chemuru","year":"2016","journal-title":"J Mol Biol"},{"key":"ref70","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1107\/S090744490000679X","article-title":"Accurate calculation of the density of proteins","volume":"56","author":"ML Quillin","year":"2000","journal-title":"Acta Crystallogr D Biol Crystallogr"}],"container-title":["PLOS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0155747","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,17]],"date-time":"2024-06-17T11:19:27Z","timestamp":1718623167000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0155747"}},"subtitle":[],"editor":[{"given":"David R","family":"Borchelt","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2016,6,6]]},"references-count":70,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2016,6,6]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0155747","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,6,6]]}}}